Open AccessPreliminary X‐ray crystallographic analysis of the catalytic domain of prophenoloxidase activating factor‐I
Author(s) -
Lee Jaewon,
Piao Shunfu,
Jung Ji Young,
Park Ji Won,
Lee Bok Leul,
Ha NamChul
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106025851
Subject(s) - crystallography , crystal structure , crystallization , molecular replacement , crystal (programming language) , materials science , chemistry , organic chemistry , computer science , programming language
Clip‐domain serine proteases (SPs) have been identified in invertebrates as crucial enzymes that are involved in diverse extracellular signalling pathways. Prophenoloxidase (proPO) activating factor‐I (PPAF‐I), a catalytically active clip‐domain SP, cleaves proPO. To date, no crystal structures of a catalytically active clip‐domain SP have been determined. Here, the results of crystallization and preliminary X‐ray analysis of the SP domain of PPAF‐I are reported. The crystal of the PPAF‐I SP domain was obtained using the hanging‐drop vapour‐diffusion method in a precipitant solution containing 0.15 M lithium sulfate, 30% polyethylene glycol 4000 and 0.1 M Tris–HCl pH 8.0. The crystal diffracts X‐rays to 1.7 Å resolution using a synchrotron‐radiation source. The crystal belongs to space group P 2 1 2 1 2 1 , with one molecule in the asymmetric unit and unit‐cell parameters a = 38.3, b = 53.3, c = 116.6 Å, α = β = γ = 90°. A molecular‐replacement solution has been found using kallikrein as a starting model, resulting in an interpretable electron‐density map.